GNL3_RAT
ID GNL3_RAT Reviewed; 538 AA.
AC Q811S9; Q566E0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Guanine nucleotide-binding protein-like 3;
DE AltName: Full=Nucleolar GTP-binding protein 3;
DE AltName: Full=Nucleostemin;
GN Name=Gnl3; Synonyms=Ns;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TP53, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=12464630; DOI=10.1101/gad.55671;
RA Tsai R.Y.L., McKay R.D.G.;
RT "A nucleolar mechanism controlling cell proliferation in stem and cancer
RT cells.";
RL Genes Dev. 16:2991-3003(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, DOMAINS, AND MUTAGENESIS OF GLY-256 AND GLY-261.
RX PubMed=15657390; DOI=10.1083/jcb.200409053;
RA Tsai R.Y.L., McKay R.D.G.;
RT "A multistep, GTP-driven mechanism controlling the dynamic cycling of
RT nucleostemin.";
RL J. Cell Biol. 168:179-184(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-505, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May be required to maintain the proliferative capacity of
CC stem cells. Stabilizes MDM2 by preventing its ubiquitination, and hence
CC proteasomal degradation (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12464630}.
CC -!- SUBUNIT: Interacts with MDM2; this interaction stabilizes MDM2.
CC Interaction with MDM2 occurs in the nucleoplasm and is triggered by a
CC nucleolar release mechanism, such as mitosis-induced nucleolar
CC disassembly (By similarity). May interact with p53/TP53 via its basic
CC domain. This interaction is most probably indirect and mediated by
CC MDM2-binding (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15657390}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12464630, ECO:0000269|PubMed:15657390}.
CC Note=Shuttles between the nucleus and nucleolus (PubMed:15657390).
CC {ECO:0000269|PubMed:15657390}.
CC -!- TISSUE SPECIFICITY: Expressed in testis. {ECO:0000269|PubMed:12464630}.
CC -!- DEVELOPMENTAL STAGE: Expressed by developing CNS stem cells. When
CC cortical stem cells differentiate into neurons, astrocytes, and
CC oligodendrocytes, expression level is reduced in both dividing and
CC postmitotic progeny.
CC -!- DOMAIN: The basic domain (B) allows nucleolar localization in the
CC absence of GTP. The intermediate domain (I) inhibits nucleolar
CC localization by the B domain and is required for exit from the
CC nucleolus. Exit from the nucleolus to the nucleoplasm requires both the
CC I and the acidic (A) domains, and may be triggered by GTP hydrolysis.
CC {ECO:0000269|PubMed:15657390}.
CC -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC characterized by a circular permutation of the GTPase motifs described
CC by a G4-G1-G3 pattern. {ECO:0000269|PubMed:15657390}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR EMBL; AY181024; AAO19471.1; -; mRNA.
DR EMBL; BC093602; AAH93602.1; -; mRNA.
DR RefSeq; NP_783170.1; NM_175580.2.
DR AlphaFoldDB; Q811S9; -.
DR SMR; Q811S9; -.
DR STRING; 10116.ENSRNOP00000035860; -.
DR iPTMnet; Q811S9; -.
DR PhosphoSitePlus; Q811S9; -.
DR jPOST; Q811S9; -.
DR PaxDb; Q811S9; -.
DR PRIDE; Q811S9; -.
DR Ensembl; ENSRNOT00000033677; ENSRNOP00000035860; ENSRNOG00000028461.
DR GeneID; 290556; -.
DR KEGG; rno:290556; -.
DR UCSC; RGD:631354; rat.
DR CTD; 26354; -.
DR RGD; 631354; Gnl3.
DR eggNOG; KOG2484; Eukaryota.
DR GeneTree; ENSGT00940000158320; -.
DR HOGENOM; CLU_011106_5_3_1; -.
DR InParanoid; Q811S9; -.
DR OMA; FKLDGLW; -.
DR OrthoDB; 1210675at2759; -.
DR PhylomeDB; Q811S9; -.
DR TreeFam; TF313085; -.
DR Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:Q811S9; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000028461; Expressed in pancreas and 19 other tissues.
DR Genevisible; Q811S9; RN.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; ISO:RGD.
DR GO; GO:0008283; P:cell population proliferation; IDA:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:1904816; P:positive regulation of protein localization to chromosome, telomeric region; ISO:RGD.
DR GO; GO:0033235; P:positive regulation of protein sumoylation; ISO:RGD.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0017145; P:stem cell division; ISO:RGD.
DR GO; GO:0019827; P:stem cell population maintenance; ISO:RGD.
DR Gene3D; 1.10.1580.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR014813; Gnl3_N_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF08701; GN3L_Grn1; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; GTP-binding; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..538
FT /note="Guanine nucleotide-binding protein-like 3"
FT /id="PRO_0000122446"
FT DOMAIN 129..307
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..46
FT /note="Basic"
FT REGION 277..451
FT /note="Intermediate"
FT REGION 460..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..532
FT /note="Acidic"
FT COILED 54..95
FT /evidence="ECO:0000255"
FT COMPBIAS 1..45
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..498
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 176..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 256..263
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305"
FT BINDING 300..303
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 79
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI11"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CI11"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BVP2"
FT MUTAGEN 256
FT /note="G->V: Abrogates GTP-binding and nucleolar
FT localization."
FT /evidence="ECO:0000269|PubMed:15657390"
FT MUTAGEN 261
FT /note="G->V: Abrogates nucleolar localization."
FT /evidence="ECO:0000269|PubMed:15657390"
SQ SEQUENCE 538 AA; 60661 MW; 936DF707F31A62CA CRC64;
MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPKKDPGV PNSAPFKEAL
LREAELRKQQ LEELKQQQKL DRQKEQERKR KLEISPDDEQ SNVETQEESD EPKIKKAKSG
KQNPKKLHCQ ELKKVIEASD IVLEVLDARD PLGCRCPQVE EAVIQSGCKK LVLVLNKSDL
VPKENLENWL TYLNKELPTV VFKASTNLKN RKKTFKIKKK VVPFQSKLCC GKEALWKLLG
GFQQSCGKGV QVGVVGFPNV GKSSIINSLK QERICSVGVS MGLTRSMQIV PLDKQITIID
SPCFIISPCN SPAALALRSP ASIEVLRPLE AASAILSQAD SQQVVLKYTV PGYKDSLDFF
TKLAQRRGLH QKGGSPNVES AAKLLWSEWT GASLGYYCHP PASWNHSPHF NENITAIMKR
GFNLEELEKN NAHSIQVLKG PHLTNKILFR SSGLTNGILE EKDIPEESPK QTEDQQDGDD
QEHVTGEKNA EISDVTPVEE TREMSPGQST ASKPSDRSFI LDKMSEEDDA YDFTTDYI
